XPO1 regulates erythroid differentiation and is a new target for the treatment of β-thalassemia

Flavia Guillem; Michaël Dussiot; Elia Colin; Thunwarat Suriyun; Jean Benoit Arlet; Nicolas Goudin; Guillaume Marcion; Renaud Seigneuric; Sebastien Causse; Patrick Gonin; Marc Gastou; Marc Deloger; Julien Rossignol; Mathilde Lamarque; Zakia Belaid Choucair; Emilie Fleur Gautier; Sarah Ducamp; Julie Vandekerckhove; Ivan C. Moura; Thiago Trovati Maciel; Carmen Garrido; Xiuli An; Patrick Mayeux; Narla Mohandas; Geneviève Courtois; Olivier Hermine

doi:10.3324/haematol.2018.210054

XPO1 regulates erythroid differentiation and is a new target for the treatment of β-thalassemia

Flavia Guillem, Michaël Dussiot, Elia Colin, Thunwarat Suriyun, Jean Benoit Arlet, Nicolas Goudin, Guillaume Marcion, Renaud Seigneuric, Sebastien Causse, Patrick Gonin, Marc Gastou, Marc Deloger, Julien Rossignol, Mathilde Lamarque, Zakia Belaid Choucair, Emilie Fleur Gautier, Sarah Ducamp, Julie Vandekerckhove, Ivan C. Moura, Thiago Trovati MacielCarmen Garrido, Xiuli An, Patrick Mayeux, Narla Mohandas, Geneviève Courtois, Olivier Hermine

Résultats de recherche: Contribution à un journal › Article › Revue par des pairs

18 Citations (Scopus)

Résumé

_β ^-thalassemia caused _{of hemoglobin,} by a quantitative ^major_leading⁽β^-TM)_to defect _the^is_accumulation in ^an the ^inherited synthesis _{of free}^{hemoglobinopathy} of _a β-globin _-globin chains _chains that aggregate and cause ineffective erythropoiesis. We have previously demonstrated that terminal erythroid maturation requires a transient activation of caspase-3 and that the chaperone Heat Shock Protein 70 (HSP70) accumulates in the nucleus to protect GATA-1 transcription factor from caspase-3 cleavage. This nuclear accumulation of HSP70 is inhibited in human β-TM erythroblasts due to HSP70 sequestration in the cytoplasm by free a-globin chains, resulting in maturation arrest and apoptosis. Likewise, terminal maturation can be restored by transduction of a nuclear-targeted HSP70 mutant.

langue originale	Anglais
Pages (de - à)	2240-2249
Nombre de pages	10
journal	Haematologica
Volume	105
Numéro de publication	9
Les DOIs	https://doi.org/10.3324/haematol.2018.210054
état	Publié - 1 sept. 2020

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10.3324/haematol.2018.210054

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Guillem, F., Dussiot, M., Colin, E., Suriyun, T., Arlet, J. B., Goudin, N., Marcion, G., Seigneuric, R., Causse, S., Gonin, P., Gastou, M., Deloger, M., Rossignol, J., Lamarque, M., Belaid Choucair, Z., Fleur Gautier, E., Ducamp, S., Vandekerckhove, J., Moura, I. C., ... Hermine, O. (2020). XPO1 regulates erythroid differentiation and is a new target for the treatment of β-thalassemia. Haematologica, 105(9), 2240-2249. https://doi.org/10.3324/haematol.2018.210054

@article{b28b783794114dd8b35eb0e25a3b8d45,

title = "XPO1 regulates erythroid differentiation and is a new target for the treatment of β-thalassemia",

abstract = "β -thalassemia caused of hemoglobin, by a quantitative majorleading(β-TM)to defect theisaccumulation in an the inherited synthesis of freehemoglobinopathy of a β-globin -globin chains chains that aggregate and cause ineffective erythropoiesis. We have previously demonstrated that terminal erythroid maturation requires a transient activation of caspase-3 and that the chaperone Heat Shock Protein 70 (HSP70) accumulates in the nucleus to protect GATA-1 transcription factor from caspase-3 cleavage. This nuclear accumulation of HSP70 is inhibited in human β-TM erythroblasts due to HSP70 sequestration in the cytoplasm by free a-globin chains, resulting in maturation arrest and apoptosis. Likewise, terminal maturation can be restored by transduction of a nuclear-targeted HSP70 mutant.",

author = "Flavia Guillem and Micha{\"e}l Dussiot and Elia Colin and Thunwarat Suriyun and Arlet, {Jean Benoit} and Nicolas Goudin and Guillaume Marcion and Renaud Seigneuric and Sebastien Causse and Patrick Gonin and Marc Gastou and Marc Deloger and Julien Rossignol and Mathilde Lamarque and {Belaid Choucair}, Zakia and {Fleur Gautier}, Emilie and Sarah Ducamp and Julie Vandekerckhove and Moura, {Ivan C.} and Maciel, {Thiago Trovati} and Carmen Garrido and Xiuli An and Patrick Mayeux and Narla Mohandas and Genevi{\`e}ve Courtois and Olivier Hermine",

note = "Publisher Copyright: {\textcopyright} 2020 Ferrata Storti Foundation",

year = "2020",

month = sep,

day = "1",

doi = "10.3324/haematol.2018.210054",

language = "English",

volume = "105",

pages = "2240--2249",

journal = "Haematologica",

issn = "0390-6078",

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Guillem, F, Dussiot, M, Colin, E, Suriyun, T, Arlet, JB, Goudin, N, Marcion, G, Seigneuric, R, Causse, S, Gonin, P, Gastou, M, Deloger, M, Rossignol, J, Lamarque, M, Belaid Choucair, Z, Fleur Gautier, E, Ducamp, S, Vandekerckhove, J, Moura, IC, Maciel, TT, Garrido, C, An, X, Mayeux, P, Mohandas, N, Courtois, G & Hermine, O 2020, 'XPO1 regulates erythroid differentiation and is a new target for the treatment of β-thalassemia', Haematologica, VOL. 105, Numéro 9, p. 2240-2249. https://doi.org/10.3324/haematol.2018.210054

TY - JOUR

T1 - XPO1 regulates erythroid differentiation and is a new target for the treatment of β-thalassemia

AU - Guillem, Flavia

AU - Dussiot, Michaël

AU - Colin, Elia

AU - Suriyun, Thunwarat

AU - Arlet, Jean Benoit

AU - Goudin, Nicolas

AU - Marcion, Guillaume

AU - Seigneuric, Renaud

AU - Causse, Sebastien

AU - Gonin, Patrick

AU - Gastou, Marc

AU - Deloger, Marc

AU - Rossignol, Julien

AU - Lamarque, Mathilde

AU - Belaid Choucair, Zakia

AU - Fleur Gautier, Emilie

AU - Ducamp, Sarah

AU - Vandekerckhove, Julie

AU - Moura, Ivan C.

AU - Maciel, Thiago Trovati

AU - Garrido, Carmen

AU - An, Xiuli

AU - Mayeux, Patrick

AU - Mohandas, Narla

AU - Courtois, Geneviève

AU - Hermine, Olivier

PY - 2020/9/1

Y1 - 2020/9/1

N2 - β -thalassemia caused of hemoglobin, by a quantitative majorleading(β-TM)to defect theisaccumulation in an the inherited synthesis of freehemoglobinopathy of a β-globin -globin chains chains that aggregate and cause ineffective erythropoiesis. We have previously demonstrated that terminal erythroid maturation requires a transient activation of caspase-3 and that the chaperone Heat Shock Protein 70 (HSP70) accumulates in the nucleus to protect GATA-1 transcription factor from caspase-3 cleavage. This nuclear accumulation of HSP70 is inhibited in human β-TM erythroblasts due to HSP70 sequestration in the cytoplasm by free a-globin chains, resulting in maturation arrest and apoptosis. Likewise, terminal maturation can be restored by transduction of a nuclear-targeted HSP70 mutant.

AB - β -thalassemia caused of hemoglobin, by a quantitative majorleading(β-TM)to defect theisaccumulation in an the inherited synthesis of freehemoglobinopathy of a β-globin -globin chains chains that aggregate and cause ineffective erythropoiesis. We have previously demonstrated that terminal erythroid maturation requires a transient activation of caspase-3 and that the chaperone Heat Shock Protein 70 (HSP70) accumulates in the nucleus to protect GATA-1 transcription factor from caspase-3 cleavage. This nuclear accumulation of HSP70 is inhibited in human β-TM erythroblasts due to HSP70 sequestration in the cytoplasm by free a-globin chains, resulting in maturation arrest and apoptosis. Likewise, terminal maturation can be restored by transduction of a nuclear-targeted HSP70 mutant.

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U2 - 10.3324/haematol.2018.210054

DO - 10.3324/haematol.2018.210054

M3 - Article

C2 - 33054049

AN - SCOPUS:85090224340

SN - 0390-6078

VL - 105

SP - 2240

EP - 2249

JO - Haematologica

JF - Haematologica

IS - 9

ER -